ID   KOJP_ECOLI              Reviewed;         755 AA.
AC   P77154;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   28-JAN-2026, entry version 154.
DE   RecName: Full=Kojibiose phosphorylase {ECO:0000303|PubMed:29684280};
DE            EC=2.4.1.230 {ECO:0000269|PubMed:29684280};
GN   Name=ycjT; OrderedLocusNames=b1316, JW1309;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX   PubMed=29684280; DOI=10.1021/acs.biochem.8b00392;
RA   Mukherjee K., Narindoshvili T., Raushel F.M.;
RT   "Discovery of a kojibiose phosphorylase in Escherichia coli K-12.";
RL   Biochemistry 57:2857-2867(2018).
CC   -!- FUNCTION: In vitro catalyzes the phosphorolysis of D-kojibiose into
CC       beta-D-glucose 1-phosphate and D-glucose. No other disaccharides tested
CC       substitute for D-kojibiose. In the reverse direction disaccharides can
CC       be formed from beta-D-glucose 1-phosphate plus D-glucose, L-sorbose, D-
CC       sorbitol, L-iditol or 1,5-anhydro-D-glucitol, but with low efficiency.
CC       The beta-D-glucose 1-phosphate product is the substrate for YcjU (AC
CC       P77366), the next apparent enzyme in the putative biochemical pathway
CC       encoded in this locus (yjcM to ycjW). {ECO:0000269|PubMed:29684280}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=kojibiose + phosphate = beta-D-glucose 1-phosphate + D-
CC         glucose; Xref=Rhea:RHEA:11176, ChEBI:CHEBI:4167, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57684, ChEBI:CHEBI:142460; EC=2.4.1.230;
CC         Evidence={ECO:0000269|PubMed:29684280};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.05 mM for kojibiose (at pH 7.5, 30 degrees Celsius)
CC         {ECO:0000269|PubMed:29684280};
CC         KM=3 mM for phosphate (at pH 7.5, 30 degrees Celsius)
CC         {ECO:0000269|PubMed:29684280};
CC         KM=1.7 mM for D-glucose (at pH 7.5, 30 degrees Celsius)
CC         {ECO:0000269|PubMed:29684280};
CC         Note=kcat is 1.0 sec(-1) for phosphorolysis of kojibiose, and kcat is
CC         0.8 sec(-1) for the reverse reaction. {ECO:0000269|PubMed:29684280};
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype when grown on glucose.
CC       {ECO:0000269|PubMed:29684280}.
CC   -!- MISCELLANEOUS: Kojibiose does not support bacterial growth of K12 /
CC       BW25113 nor of BL-21(DE3), perhaps because it is not transported into
CC       E.coli. {ECO:0000269|PubMed:29684280}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74398.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14891.1; -; Genomic_DNA.
DR   PIR; G64880; G64880.
DR   RefSeq; NP_415832.1; NC_000913.3.
DR   RefSeq; WP_000198036.1; NZ_CP009789.1.
DR   AlphaFoldDB; P77154; -.
DR   SMR; P77154; -.
DR   BioGRID; 4263194; 20.
DR   FunCoup; P77154; 97.
DR   IntAct; P77154; 1.
DR   STRING; 511145.b1316; -.
DR   CAZy; GH65; Glycoside Hydrolase Family 65.
DR   PaxDb; 511145-b1316; -.
DR   EnsemblBacteria; AAC74398; AAC74398; b1316.
DR   GeneID; 945895; -.
DR   KEGG; ecj:JW1309; -.
DR   KEGG; eco:b1316; -.
DR   KEGG; ecoc:C3026_07710; -.
DR   PATRIC; fig|1411691.4.peg.963; -.
DR   EchoBASE; EB3676; -.
DR   eggNOG; COG1554; Bacteria.
DR   HOGENOM; CLU_006285_2_1_6; -.
DR   InParanoid; P77154; -.
DR   OMA; EAYCIPF; -.
DR   OrthoDB; 9816160at2; -.
DR   PhylomeDB; P77154; -.
DR   BioCyc; EcoCyc:G6654-MONOMER; -.
DR   BioCyc; MetaCyc:G6654-MONOMER; -.
DR   BRENDA; 2.4.1.230; 2026.
DR   SABIO-RK; P77154; -.
DR   STRENDA-DB; 0TOYQL; Determination of Phosphorylase and hydrolase activity of YcjT.
DR   PRO; PR:P77154; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0033831; F:kojibiose phosphorylase activity; IDA:EcoCyc.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR037018; GH65_N.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR   PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..755
FT                   /note="Kojibiose phosphorylase"
FT                   /id="PRO_0000108017"
FT   ACT_SITE        473
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         333..334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         573..574
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ   SEQUENCE   755 AA;  84867 MW;  89A645A7A5AB599D CRC64;
     MTRPVTLSEP HFSQHTLNKY ASLMAQGNGY LGLRASHEED YTRQTRGMYL AGLYHRAGKG
     EINELVNLPD VVGMEIAING EVFSLSHEAW QRELDFASGE LRRNVVWRTS NGSGYTIASR
     RFVSADQLPL IALEITITPL DADASVLIST GIDATQTNHG RQHLDETQVR VFGQHLMQGS
     YTTQDGRSDV AISCCCKVSG DVQQCYTAKE RRLLQHTSAQ LHAGETMTLQ KLVWIDWRDD
     RQAALDEWGS ASLRQLEMCA QQSYDQLLAA STENWRQWWQ KRRITVNGGE AHDQQALDYA
     LYHLRIMTPA HDERSSIAAK GLTGEGYKGH VFWDTEVFLL PFHLFSDPTV ARSLLRYRWH
     NLPGAQEKAR RNGWQGALFP WESARSGEEE TPEFAAINIR TGLRQKVASA QAEHHLVADI
     AWAVIQYWQT TGDESFIAHE GMALLLETAK FWISRAVRVN DRLEIHDVIG PDEYTEHVNN
     NAYTSYMARY NVQQALNIAR QFGCSDDAFI HRAEMFLKEL WMPEIQPDGV LPQDDSFMAK
     PAINLAKYKA AAGKQTILLD YSRAEVNEMQ ILKQADVVML NYMLPEQFSA ASCLANLQFY
     EPRTIHDSSL SKAIHGIVAA RCGLLTQSYQ FWREGTEIDL GADPHSCDDG IHAAATGAIW
     LGAIQGFAGV SVRDGELHLN PALPEQWQQL SFPLFWQGCE LQVTLDAQRI AIRTSAPVSL
     RLNGQLITVA EESVFCLGDF ILPFNGTATK HQEDE
//